lipoprotein B, partial [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Periplasmic_Binding_Protein_Type_2 super family | cl21456 | Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ... |
95-151 | 8.97e-03 | ||
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences. The actual alignment was detected with superfamily member cd13675: Pssm-ID: 473866 [Multi-domain] Cd Length: 296 Bit Score: 35.31 E-value: 8.97e-03
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| Name | Accession | Description | Interval | E-value | ||
| PBP2_TRAP_SBP_like_5 | cd13675 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
95-151 | 8.97e-03 | ||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270393 [Multi-domain] Cd Length: 296 Bit Score: 35.31 E-value: 8.97e-03
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| Name | Accession | Description | Interval | E-value | ||
| PBP2_TRAP_SBP_like_5 | cd13675 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
95-151 | 8.97e-03 | ||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270393 [Multi-domain] Cd Length: 296 Bit Score: 35.31 E-value: 8.97e-03
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